Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Trithorax group protein osa

Gene

osa

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Trithorax group (trxG) protein required for embryonic segmentation, development of the notum and wing margin, and photoreceptor differentiation. Required for the activation of genes such as Antp, Ubx and Eve. Binds to DNA without specific affinity, suggesting that it is recruited to promoters by promoter-specific proteins. Essential component of the Brahma complex, a multiprotein complex which is the equivalent of the yeast SWI/SNF complex and acts by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. This complex can both serve as a transcriptional coactivator or corepressor, depending on the context. Acts as an essential coactivator for Zeste, which recruits the whole complex to specific genes. In contrast, it acts as a corepressor for Wg target genes, possibly via an interaction with Pan and Gro. It also acts as a negative regulator for proneural achaete-scute, when it is directly recruited by Pan and Chi. Also represses E2f activation.6 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB

GO - Biological processi

  • adult chitin-containing cuticle pigmentation Source: FlyBase
  • chromatin remodeling Source: InterPro
  • imaginal disc-derived leg morphogenesis Source: FlyBase
  • imaginal disc-derived wing margin morphogenesis Source: UniProtKB
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • imaginal disc-derived wing vein morphogenesis Source: FlyBase
  • negative regulation of neuroblast proliferation Source: FlyBase
  • neuroblast fate commitment Source: FlyBase
  • neurogenesis Source: FlyBase
  • photoreceptor cell differentiation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: FlyBase
  • regulation of epidermal growth factor receptor signaling pathway Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • segment specification Source: UniProtKB
  • sensory perception of pain Source: FlyBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • wing disc dorsal/ventral pattern formation Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-DME-3214858. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Trithorax group protein osa
Alternative name(s):
Protein eyelid
Gene namesi
Name:osa
Synonyms:eld
ORF Names:CG7467
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0261885. osa.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  • brahma complex Source: FlyBase
  • nucleoplasm Source: FlyBase
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27162716Trithorax group protein osaPRO_0000200593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841Phosphothreonine1 Publication
Modified residuei747 – 7471Phosphothreonine1 Publication
Modified residuei1930 – 19301Phosphoserine1 Publication
Modified residuei1932 – 19321Phosphoserine1 Publication
Modified residuei2081 – 20811Phosphoserine1 Publication
Modified residuei2168 – 21681Phosphoserine1 Publication
Modified residuei2169 – 21691Phosphoserine1 Publication
Modified residuei2176 – 21761Phosphothreonine1 Publication
Modified residuei2181 – 21811Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8IN94.
PRIDEiQ8IN94.

PTM databases

iPTMnetiQ8IN94.

Expressioni

Tissue specificityi

Ubiquitously expressed in early embryo. In third instar larvae, it is ubiquitously expressed in wing and eye-antenna imaginal disks, with a stronger expression in a band just anterior to the morphogenetic furrow.1 Publication

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Gene expression databases

BgeeiQ8IN94.
ExpressionAtlasiQ8IN94. differential.
GenevisibleiQ8IN94. DM.

Interactioni

Subunit structurei

Component of the Brahma complex, which is composed of Brm, Osa, Mor, Snr1/Bap45, Bap111/Dalao, Bap55, Bap60 and Bap47. Interacts with Pnr and Chi via its EHD domain.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
brmP254394EBI-115993,EBI-868480

Protein-protein interaction databases

BioGridi67162. 25 interactions.
DIPiDIP-20699N.
IntActiQ8IN94. 6 interactions.
MINTiMINT-297379.
STRINGi7227.FBpp0088543.

Structurei

3D structure databases

ProteinModelPortaliQ8IN94.
SMRiQ8IN94. Positions 993-1088.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1000 – 109192ARIDPROSITE-ProRule annotationAdd
BLAST
Domaini1769 – 2517749EHDAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 17631745Pro-richAdd
BLAST
Compositional biasi174 – 380207Gln-richAdd
BLAST
Compositional biasi619 – 873255Gly-richAdd
BLAST
Compositional biasi1222 – 1453232Gly-richAdd
BLAST
Compositional biasi1271 – 1751481Gln-richAdd
BLAST
Compositional biasi1730 – 174516His-richAdd
BLAST
Compositional biasi2589 – 262436Ser-richAdd
BLAST
Compositional biasi2625 – 271692Ala-richAdd
BLAST

Domaini

The ARID domains mediates the binding to DNA.

Sequence similaritiesi

Contains 1 ARID domain.PROSITE-ProRule annotation
Contains 1 EHD (Eyelid homology) domain.Curated

Phylogenomic databases

eggNOGiKOG2510. Eukaryota.
ENOG410Y034. LUCA.
GeneTreeiENSGT00550000074575.
InParanoidiQ8IN94.
KOiK11653.
OMAiMDDMLSS.
OrthoDBiEOG7M6D7M.
PhylomeDBiQ8IN94.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
IPR016024. ARM-type_fold.
IPR021906. BAF250/Osa.
IPR033388. BAF250_C.
[Graphical view]
PANTHERiPTHR12656. PTHR12656. 7 hits.
PfamiPF01388. ARID. 1 hit.
PF12031. DUF3518. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF48371. SSF48371. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IN94-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEKIKSPQT QQQQQGGAPA PAATPPSAGA APGAATPPTS GPPTPNNNSN
60 70 80 90 100
NGSDPSIQQQ QQNVAPHPYG APPPPGSGPG GPPGPDPAAV MHYHHLHQQQ
110 120 130 140 150
QQHPPPPHMQ QQQHHGGPAP PPPGGAPEHA PGVKEEYTHL PPPHPHPAYG
160 170 180 190 200
RYHADPNMDP YRYGQPLPGG KPPQQQQPHP QQQPPQQPGP GGSPNRPPQQ
210 220 230 240 250
RYIPGQPPQG PTPTLNSLLQ SSNPPPPPQH RYANTYDPQQ AAASAAAAAA
260 270 280 290 300
AQQQQAGGPP PPGHGPPPPQ HQPSPYGGQQ GGWAPPPRPY SPQLGPSQQY
310 320 330 340 350
RTPPPTNTSR GQSPYPPAHG QNSGSYPSSP QQQQQQQQQQ QQQAGQQPGG
360 370 380 390 400
PVPGGPPPGT GQQPPQQNTP PTSQYSPYPQ RYPTPPGLPA GGSNHRTAYS
410 420 430 440 450
THQYPEPNRP WPGGSSPSPG SGHPLPPASP HHVPPLQQQP PPPPHVSAGG
460 470 480 490 500
PPPSSSPGHA PSPSPQPSQA SPSPHQELIG QNSNDSSSGG AHSGMGSGPP
510 520 530 540 550
GTPNPQQVMR PTPSPTGSSG SRSMSPAVAQ NHPISRPASN QSSSGGPMQQ
560 570 580 590 600
PPVGAGGPPP MPPHPGMPGG PPQQQQSQQQ QASNSASSAS NSPQQTPPPA
610 620 630 640 650
PPPNQGMNNM ATPPPPPQGA AGGGYPMPPH MHGGYKMGGP GQSPGAQGYP
660 670 680 690 700
PQQPQQYPPG NYPPRPQYPP GAYATGPPPP PTSQAGAGGA NSMPSGAQAG
710 720 730 740 750
GYPGRGMPNH TGQYPPYQWV PPSPQQTVPG GAPGGAMVGN HVQGKGTPPP
760 770 780 790 800
PVVGGPPPPQ GSGSPRPLNY LKQHLQHKGG YGGSPTPPQG PQGYGNGPTG
810 820 830 840 850
MHPGMPMGPP HHMGPPHGPT NMGPPTSTPP QSQMLQGGQP QGQGASGGPE
860 870 880 890 900
SGGPEHISQD NGISSSGPTG AAGMHAVTSV VTTGPDGTSM DEVSQQSTLS
910 920 930 940 950
NASAASGEDP QCTTPKSRKN DPYSQSHLAP PSTSPHPVVM HPGGGPGEEY
960 970 980 990 1000
DMSSPPNWPR PAGSPQVFNH VPVPQEPFRS TITTTKKSDS LCKLYEMDDN
1010 1020 1030 1040 1050
PDRRGWLDKL RAFMEERRTP ITACPTISKQ PLDLYRLYIY VKERGGFVEV
1060 1070 1080 1090 1100
TKSKTWKDIA GLLGIGASSS AAYTLRKHYT KNLLTFECHF DRGDIDPLPI
1110 1120 1130 1140 1150
IQQVEAGSKK KTAKAASVPS PGGGHLDAGT TNSTGSSNSQ DSFPAPPGSA
1160 1170 1180 1190 1200
PNAAIDGYPG YPGGSPYPVA SGPQPDYATA GQMQRPPSQN NPQTPHPGAA
1210 1220 1230 1240 1250
AAVAAGDNIS VSNPFEDPIA AGGGPGSGTG PGPGQGPGPG AASGGAGAVG
1260 1270 1280 1290 1300
AVGGGPQPHP PPPHSPHTAA QQAAGQHQQQ HPQHQHPGLP GPPPPQQQQG
1310 1320 1330 1340 1350
QQGQQPPPSV GGGPPPAPQQ HGPGQVPPSP QQHVRPAAGA PYPPGGSGYP
1360 1370 1380 1390 1400
TPVSRTPGSP YPSQPGAYGQ YGSSDQYNAT GPPGQPFGQG PGQYPPQNRN
1410 1420 1430 1440 1450
MYPPYGPEGE APPTGANQYG PYGSRPYSQP PPGGPQPPTQ TVAGGPPAGG
1460 1470 1480 1490 1500
APGAPPSSAY PTGRPSQQDY YQPPPDQSPQ PRRHPDFIKD SQPYPGYNAR
1510 1520 1530 1540 1550
PQIYGAWQSG TQQYRPQYPS SPAPQNWGGA PPRGAAPPPG APHGPPIQQP
1560 1570 1580 1590 1600
AGVAQWDQHR YPPQQGPPPP PQQQQQPQQQ QQQPPYQQVA GPPGQQPPQA
1610 1620 1630 1640 1650
PPQWAQMNPG QTAQSGIAPP GSPLRPPSGP GQQNRMPGMP AQQQQSQQQG
1660 1670 1680 1690 1700
GVPQPPPQQA SHGGVPSPGL PQVGPGGMVK PPYAMPPPPS QGVGQQVGQG
1710 1720 1730 1740 1750
PPGGMMSQKP PPMPGQAMQQ QPLQQQPPSH QHPHPHQHPQ HQHPHQMPPN
1760 1770 1780 1790 1800
QTAPGGYGPP GMPGGGAQLV KKELIFPHDS VESTTPVLYR RKRLMKADVC
1810 1820 1830 1840 1850
PVDPWRIFMA MRSGLLTECT WALDVLNVLL FDDSTVQFFG ISNLPGLLTL
1860 1870 1880 1890 1900
LLEHFQKNLA EMFDERENEE QSALLAEDAD DDADSGTVMC EKLRTSGRQP
1910 1920 1930 1940 1950
RCVRSISSYN RRRHYENMDR SGKDGAGNGS DSEDADEGID LGQVRVQPNP
1960 1970 1980 1990 2000
EERSLLLSFT PNYTMVTRKG VPVRIQPAEN DIFVDERQKA WDIDTNRLYE
2010 2020 2030 2040 2050
QLEPVGSDAW TYGFTEPDPL DGIIDVFKSE IVNIPFARYI RSDKKGRKRT
2060 2070 2080 2090 2100
ELASSSRKPE IKTEENSTEE QTFNKKRRLV SGGSSSSGAH AEGKKSKLTS
2110 2120 2130 2140 2150
EEFAQPNAEV KKEPGTADSD CRPVDMDIEA PQQRLTNGVA PCSSTPAIFD
2160 2170 2180 2190 2200
PRTTAKDEAR VLQRRRDSSF EDECYTRDEA SLHLVSESQD SLARRCIALS
2210 2220 2230 2240 2250
NIFRNLTFVP GNETVLAKST RFLAVLGRLL LLNHEHLRRT PKTRNYDREE
2260 2270 2280 2290 2300
DTDFSDSCSS LQGEREWWWD YLITIRENML VAMANIAGHL ELSRYDELIA
2310 2320 2330 2340 2350
RPLIDGLLHW AVCPSAHGQD PFPSCGPNSV LSPQRLALEA LCKLCVTDAN
2360 2370 2380 2390 2400
VDLVIATPPF SRLEKLCAVL TRHLCRNEDQ VLREFSVNLL HYLAAADSAM
2410 2420 2430 2440 2450
ARTVALQSPC ISYLVAFIEQ AEQTALGVAN QHGINYLREN PDSMGTSLDM
2460 2470 2480 2490 2500
LRRAAGTLLH LAKHPDNRSL FMQQEQRLLG LVMSHILDQQ VALIISRVLY
2510 2520 2530 2540 2550
QVSRGTGPIH SVEFRLLQQR QQQQLRPGPA GKQAASAGGS ATVKAETAST
2560 2570 2580 2590 2600
ETSSTEAKPA PAATTAVVND ENSNSSQQLP PAATFNDVSN SSTNSNSCGT
2610 2620 2630 2640 2650
ASSNQTNNST TNSSHSSSAI SSQSAITVAA PSAAATGAGS ATAAAIASDQ
2660 2670 2680 2690 2700
QQVSKVAAAA AAAAALSNAS AAAAAAAAAA AASVGPPTSS SVSAGAAVAQ
2710
PAAPPPTNAG TTTAVA
Length:2,716
Mass (Da):284,064
Last modified:March 1, 2003 - v1
Checksum:iEFAE76CB51C7C675
GO

Sequence cautioni

The sequence AAF55457.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611Missing in AAC06254 (PubMed:9271118).Curated
Sequence conflicti1169 – 11691V → G in AAC06254 (PubMed:9271118).Curated
Sequence conflicti1795 – 17951M → T in AAC06254 (PubMed:9271118).Curated
Sequence conflicti2637 – 26371G → E in AAC06254 (PubMed:9271118).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053091 mRNA. Translation: AAC06254.1.
AE014297 Genomic DNA. Translation: AAF55457.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAN13750.1.
PIRiT13049.
RefSeqiNP_001163639.1. NM_001170168.2.
NP_524392.2. NM_079668.3.
NP_732263.1. NM_169775.2.
UniGeneiDm.2989.

Genome annotation databases

EnsemblMetazoaiFBtr0089581; FBpp0088543; FBgn0261885.
FBtr0301487; FBpp0290702; FBgn0261885.
GeneIDi42130.
KEGGidme:Dmel_CG7467.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053091 mRNA. Translation: AAC06254.1.
AE014297 Genomic DNA. Translation: AAF55457.1. Sequence problems.
AE014297 Genomic DNA. Translation: AAN13750.1.
PIRiT13049.
RefSeqiNP_001163639.1. NM_001170168.2.
NP_524392.2. NM_079668.3.
NP_732263.1. NM_169775.2.
UniGeneiDm.2989.

3D structure databases

ProteinModelPortaliQ8IN94.
SMRiQ8IN94. Positions 993-1088.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67162. 25 interactions.
DIPiDIP-20699N.
IntActiQ8IN94. 6 interactions.
MINTiMINT-297379.
STRINGi7227.FBpp0088543.

PTM databases

iPTMnetiQ8IN94.

Proteomic databases

PaxDbiQ8IN94.
PRIDEiQ8IN94.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089581; FBpp0088543; FBgn0261885.
FBtr0301487; FBpp0290702; FBgn0261885.
GeneIDi42130.
KEGGidme:Dmel_CG7467.

Organism-specific databases

CTDi42130.
FlyBaseiFBgn0261885. osa.

Phylogenomic databases

eggNOGiKOG2510. Eukaryota.
ENOG410Y034. LUCA.
GeneTreeiENSGT00550000074575.
InParanoidiQ8IN94.
KOiK11653.
OMAiMDDMLSS.
OrthoDBiEOG7M6D7M.
PhylomeDBiQ8IN94.

Enzyme and pathway databases

ReactomeiR-DME-3214858. RMTs methylate histone arginines.

Miscellaneous databases

ChiTaRSiosa. fly.
GenomeRNAii42130.
PROiQ8IN94.

Gene expression databases

BgeeiQ8IN94.
ExpressionAtlasiQ8IN94. differential.
GenevisibleiQ8IN94. DM.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
IPR016024. ARM-type_fold.
IPR021906. BAF250/Osa.
IPR033388. BAF250_C.
[Graphical view]
PANTHERiPTHR12656. PTHR12656. 7 hits.
PfamiPF01388. ARID. 1 hit.
PF12031. DUF3518. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF48371. SSF48371. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Eyelid antagonizes wingless signaling during Drosophila development and has homology to the Bright family of DNA-binding proteins."
    Treisman J.E., Luk A., Rubin G.M., Heberlein U.
    Genes Dev. 11:1949-1962(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "The trithorax group gene osa encodes an ARID-domain protein that genetically interacts with the brahma chromatin-remodeling factor to regulate transcription."
    Vazquez M., Moore L., Kennison J.A.
    Development 126:733-742(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  5. "Osa associates with the Brahma chromatin remodeling complex and promotes the activation of some target genes."
    Collins R.T., Furukawa T., Tanese N., Treisman J.E.
    EMBO J. 18:7029-7040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM AND SNR1.
  6. "A genetic screen for modifiers of E2F in Drosophila melanogaster."
    Staehling-Hampton K., Ciampa P.J., Brook A., Dyson N.
    Genetics 153:275-287(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The Drosophila brahma complex is an essential coactivator for the trithorax group protein zeste."
    Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.
    Genes Dev. 14:1058-1071(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM; OSA; MOR; SNR1; DALAO; BAP55; BAP60 AND BAP47, FUNCTION AS A COACTIVATOR.
  8. "Osa-containing Brahma chromatin remodeling complexes are required for the repression of wingless target genes."
    Collins R.T., Treisman J.E.
    Genes Dev. 14:3140-3152(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A COREPRESSOR.
  9. "Enhancer-promoter communication mediated by Chip during Pannier-driven proneural patterning is regulated by Osa."
    Heitzler P., Vanolst L., Biryukova I., Ramain P.
    Genes Dev. 17:591-596(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A COREPRESSOR, INTERACTION WITH PNR AND CHI.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-384; THR-747; SER-1930; SER-1932; SER-2081; SER-2168; SER-2169; THR-2176 AND SER-2181, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiOSA_DROME
AccessioniPrimary (citable) accession number: Q8IN94
Secondary accession number(s): O61603, Q9VEG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.